1up9: Difference between revisions

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[[Category: tetraheme cytochrome c]]
[[Category: tetraheme cytochrome c]]


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Revision as of 17:03, 30 October 2007

File:1up9.gif


1up9, resolution 1.35Å

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REDUCED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 AT PH 7.6

OverviewOverview

The tetraheme cytochrome c3 is a small metalloprotein with ca. 13,000 Da, found in sulfate-reducing bacteria, which is believed to act as a partner, of hydrogenase. The three-dimensional structure of the oxidized and, reduced forms of cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774, at pH 7.6 were determined using high-resolution X-ray crystallography and, were compared with the previously determined oxidized form at pH 4.0., Theoretical calculations were performed with both structures, using, continuum electrostatic calculations and Monte Carlo sampling of, protonation and redox states, in order to understand the molecular basis, of the redox-Bohr and cooperativity effects related to the coupled, transfer of electrons and protons. We were able to identify groups that, showed ... [(full description)]

About this StructureAbout this Structure

1UP9 is a [Single protein] structure of sequence from [Desulfovibrio desulfuricans] with SO4 and HEC as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Molecular basis for redox-Bohr and cooperative effects in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies of oxidized and reduced high-resolution structures at pH 7.6., Bento I, Matias PM, Baptista AM, da Costa PN, van Dongen WM, Saraiva LM, Schneider TR, Soares CM, Carrondo MA, Proteins. 2004 Jan 1;54(1):135-52. PMID:14705030

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